Results 71 to 80 of about 1,555,922 (344)

Microbiome−host proteostasis crosstalk—An emerging perspective on mechanisms and interventions toward healthy longevity

open access: yesFEBS Letters, EarlyView.
Proteostasis and the gut microbiota play a key role in shaping host physiology. Microbiota‐derived metabolites, vitamins, and RNA modulate host proteostasis. Findings from model systems, including C. elegans, indicate microbes can either stabilize or disrupt host proteostasis.
Abhishek Anil Dubey, Maria Ermolaeva
wiley   +1 more source

Plasma Amyloid-β Oligomerization Tendency Predicts Amyloid PET Positivity

open access: yesClinical Interventions in Aging, 2021
Jung-Min Pyun,1 Ji Sun Ryu,2 Ryan Lee,2 Kyu Hawn Shim,3 Young Chul Youn,4 Nayoung Ryoo,5 Sang-Won Han,5 Young Ho Park,5 Sungmin Kang,2 Seong Soo A An,6 SangYun Kim5 1Department of Neurology, Uijeongbu Eulji Medical Center, Eulji University, Uijeongbu-si,
Pyun JM   +10 more
doaj  

The Effect of 24-Hydroxy Cholesterol on Production of Reactive Oxygen Species (ROS) in Cultured Astrocytes Treated by Beta Amyloid

open access: yesمجله دانشکده پزشکی اصفهان, 2018
Background: Alzheimer's disease is a neurodegenerative disorder characterized by the accumulation of beta-amyloid plaques outside the cells, and intracellular hyperphosphorylation of tau protein.
Zahra Nazeri   +4 more
doaj   +1 more source

Neurotoxicity of amyloid β proteins

open access: yesFolia Pharmacologica Japonica, 2008
アミロイドβタンパク(Aβ)はアミロイド前駆タンパク(APP)からβ-およびγ-セクレターゼによってペプチド分解されて生成され,Aβオリゴマーとなって神経細胞毒性を生じる.細胞外のAβ沈着に先立って細胞内に主にAβ1-42が蓄積し,神経細胞傷害をきたす.細胞内Aβの起源として,細胞内産生よりも細胞外に分泌されたAβが細胞内に取り込まれる経路が優位であると考えられている.細胞外Aβによる神経細胞毒性機構としてNMDA受容体の細胞内取り込み増加によるシナプス機能障害やグリア細胞の活性化が報告されている.一方,細胞内Aβによる神経細胞毒性機構としてこれまでに,1)ユビキチン依存性タンパク分解の抑制,2)シナプス機能障害,3)過リン酸化タウタンパクの増加,4)カルシウム仮説,5 ...
Hattori, Naoki   +3 more
openaire   +3 more sources

Amyloid and tau in the brain in sporadic Alzheimer’s disease: defining the chicken and the egg [PDF]

open access: yes, 2014
In the October 2013 issue of Acta Neuropathologica there were three very interesting articles on: Amyloid or tau: the chicken or the egg? In the first article, David Mann and John Hardy argued that the deposition of aggregated amyloid β (Aβ) protein in ...
Cheryl A. Hawkes   +5 more
core   +1 more source

Chameleon sequences reveal structural effects in proteins representing micelle‐like distribution of hydrophobicity

open access: yesFEBS Open Bio, EarlyView.
Amino acids sequence of two different proteins with the same sequence (chameleon sequence—black boxes) represent in 3D structure of the proteins different secondary structures: HHHH—helical and BBB—Beta‐structural. The chains folded in water environment adopt different III‐order structures in which the chameleon fragments appear to adopt similar status
Irena Roterman   +4 more
wiley   +1 more source

In-vitro interaction studies between the amyloid PET tracer florbetaben and the amyloid-beta targeting antibodies lecanemab and donanemab on AD brain samples reveal no interferences

open access: yesAlzheimer’s Research & Therapy
Background Amyloid PET imaging enables the in vivo visualization and quantification of amyloid-beta deposits in the brain. In research and clinical settings, it is further used to monitor amyloid-beta burden as well as the biological response to disease ...
Andre Mueller   +9 more
doaj   +1 more source

Obstructive sleep apnea and amyloid-β42 in adolescents: The results of a pilot study

open access: yesActa Biomedica Scientifica, 2022
Background. Obstructive sleep apnea (OSA) is a chronic condition characterized by repetitive collapse of the upper airway during sleep leading to intermittent hypoxia, excessive arousals and disrupt of sleep homeostasis. OSA is associated with obesity as
O. N. Berdina   +4 more
doaj   +1 more source

Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models.

open access: yesCell, 2010
Alzheimer's disease (AD) is characterized by amyloid-beta (Abeta) and tau deposition in brain. It has emerged that Abeta toxicity is tau dependent, although mechanistically this link remains unclear. Here, we show that tau, known as axonal protein, has a
L. Ittner   +13 more
semanticscholar   +1 more source

Large‐scale bidirectional arrayed genetic screens identify OXR1 and EMC4 as modifiers of αSynuclein aggregation

open access: yesFEBS Open Bio, EarlyView.
Activation of the mitochondrial protein OXR1 increases pSyn129 αSynuclein aggregation by lowering ATP levels and altering mitochondrial membrane potential, particularly in response to MSA‐derived fibrils. In contrast, ablation of the ER protein EMC4 enhances autophagic flux and lysosomal clearance, broadly reducing α‐synuclein aggregates.
Sandesh Neupane   +11 more
wiley   +1 more source

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